Das eif5a-Epitop jenseits biologischer Resiktrikionen - Synthese & funktionelle Analytik

Within the scope of this work peptides derived from the eif5a-protein were synthesized in such a manner that these peptides showed a fixed beta-hairpin conformation in solution. The so derived peptides were then tested for their biological effects via confocal microscopy and flow cytometry. In flow cytometry experiments the peptides showed a high affinity towards monocytes, bearing the opportunity of using these structures as potential tuberculosis drugs. Structural elucidation was performed by modern 2D-NMR techniques. Furthermore it was investigated how structure and size have an impact on the dynamic and rigidity of the peptide epitopes in solution. While increasing the peptides sizes, five cysteine residues could be incoperated and still result in a regioselective, intramolecular disulfide oxidation. Modular mutations via the incoperation of new functional amino acids lead to the syntheses of supramolecular aggregates, for instance the use of metal-chelating amino acid allowed the reversible trimersation of peptide residues in aqeous media by the addition of Ga3+. Punctual Alanine-mutations allowed the development of a detailed, threedimensional structure of these peptides.